Identification of tryptophanyl residues involved in binding of carbohydrate ligands to barley α-amylase 2
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02907525.pdf
Reference39 articles.
1. Barman, T. E. &D. E. Koshland, Jr.: A colorimetric procedure for the quantitative determination of tryptophan residues in proteins. J. Biol. Chem. 242, 5771–5776 (1967)
2. Brown, A. H. D. &J. V. Jacobsen: Genetic basis and natural variation of α-amylase isozymes in barley. Genet. Res. Camb. 40, 315–324 (1982)
3. Chandler, P. M., J. A. Zwar, J. V. Jacobsen, T. J. V. Higgins &A. S. Inglis: The effects of giberellic acid and abscisic acid on α-amylase mRNA levels in barley aleurone layers studies using an α-amylase cDNA clone. Plant Mol. Biol. 3, 407–418 (1984)
4. Clarke, A. J. &B. Svensson: The role of tryptophanyl residues in the function of Aspergillus niger glucoamylase G1 and G2. Carlsberg Res. Commun. 49, 111–122 (1984)
5. Clarke, A. J. &B. Svensson: Identification of an essential tryptophanyl residue in the primary structure of glucoamylase G2 from Aspergillus niger. Carlsberg Res. Commun. 49, 559–566 (1984)
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